{PDOC51703}
{PS51703; DZF}
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* DZF domain profile *
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The DZF  domain (domain associated with zinc fingers) is a dimerization domain
found in [1,2,3]:

 - Vertebrate  nuclear factor 90 (NF90, also known as ILF3, DRBP76 or NFAR-1),
   contains two  double-stranded RNA-binding motifs (dsRBMs) (see <PDOC50137>)
   and interacts  with  highly  structured RNAs as well as the dsRNA-activated
   protein kinase (PKR).
 - Metazoan  NF45 (also known as ILF2), appears to function predominantly as a
   heterodimeric complex with NF90.
 - Vertebrate  spermatid  perinuclear RNA-binding protein (SPNR, also known as
   STRBP), a testes specific paralogue of NF90.
 - Metazoan Zinc-finger protein associated with RNA (Zfr).

Nuclear factors  NF90 and NF45 form a protein complex involved in a variety of
cellular processes  and  are  thought  to  affect  gene expression both at the
transcriptional and translational level. In addition, this complex affects the
replication of  several  viruses  through  direct interactions with viral RNA.
NF90 and  NF45  dimerize through their common DZF domain. The DZF domain shows
structural similarity  to  the  template-free nucleotidyltransferase family of
RNA modifying  enzymes.  However,  the  lack  of  conserved catalytic residues
suggests that  the  DZF domain encodes a 'pseudotransferase' that is no longer
able to catalyze transfer of nucleotides.

The DZF  dimerization  domain form an oblong structure with a flat face on one
side and  a  curved  face  on  the  other.  The  DZF  domain  is bipartite and
characterized by an N-terminal mixed alpha-beta region that contains a central
anti-parallel beta-sheet   and   a   C-terminal   alpha-helical   region  (see
<PDB:4AT7>). The  overall structure has a pseudo two-fold rotational symmetry.
The central beta-sheet forms the base of a cleft between the N- and C-terminal
halves while  dimerization  is mediated by the alpha-helices at the C-terminus
[3].

The profile we developed covers the entire DZF domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: February 2014 / First entry.

[ 1] Parker L.M., Fierro-Monti I., Mathews M.B.
     "Nuclear factor 90 is a substrate and regulator of the eukaryotic
     initiation factor 2 kinase double-stranded RNA-activated protein
     kinase."
     J. Biol. Chem. 276:32522-32530(2001).
     PubMed=11438540; DOI=10.1074/jbc.M104408200
[ 2] Doerks T., Copley R.R., Schultz J., Ponting C.P., Bork P.
     "Systematic identification of novel protein domain families associated
     with nuclear functions."
     Genome Res. 12:47-56(2002).
     PubMed=11779830; DOI=10.1101/
[ 3] Wolkowicz U.M., Cook A.G.
     "NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that
     has a nucleotidyltransferase fold."
     Nucleic Acids Res. 40:9356-9368(2012).
     PubMed=22833610; DOI=10.1093/nar/gks696

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